ERG7/YHR072W Literature Guide Help

Other names published for ERG7: lanosterol synthase ERG7, YHR072W

ERG7 - Protein Sequence Features (13)

ReferenceOther Genes Addressed
Layer JV, et al.  (2013) Characterization of a mutation that results in independence of oxidosqualene cyclase (Erg7) activity from the downstream 3-ketoreductase (Erg27) in the yeast ergosterol biosynthetic pathway. Biochim Biophys Acta 1831(2):361-9
Chang CH, et al.  (2012) The cysteine 703 to isoleucine or histidine mutation of the oxidosqualene-lanosterol cyclase from Saccharomyces cerevisiae generates an iridal-type triterpenoid. Biochimie 94(11):2376-81
Oliaro-Bosso S, et al.  (2011) Characterization of the channel constriction allowing the access of the substrate to the active site of yeast oxidosqualene cyclase. PLoS One 6(7):e22134
Wu TK, et al.  (2011) Mutation of isoleucine 705 of the oxidosqualene-lanosterol cyclase from Saccharomyces cerevisiae affects lanosterol's C/D-ring cyclization and 17alpha/beta-exocyclic side chain stereochemistry. Org Biomol Chem 9(4):1092-7
Wu TK, et al.  (2008) Protein plasticity: a single amino acid substitution in the Saccharomyces cerevisiae oxidosqualene-lanosterol cyclase generates protosta-13(17),24-dien-3beta-ol, a rearrangement product. Org Lett 10(12):2529-32
Wu TK, et al.  (2006) Phenylalanine 445 within Oxidosqualene-Lanosterol Cyclase from Saccharomyces cerevisiae Influences C-Ring Cyclization and Deprotonation Reactions. Org Lett 8(21):4691-4
Wu TK, et al.  (2006) Site-Saturated Mutagenesis of Histidine 234 of Saccharomyces cerevisiae Oxidosqualene-Lanosterol Cyclase Demonstrates Dual Functions in Cyclization and Rearrangement Reactions. J Am Chem Soc 128(19):6414-9
Oliaro-Bosso S, et al.  (2005) Access of the Substrate to the Active Site of Yeast Oxidosqualene Cyclase: An Inhibition and Site-Directed Mutagenesis Approach. Chembiochem 6(12):2221-2228
Wu TK, et al.  (2005) Histidine residue at position 234 of oxidosqualene-lanosterol cyclase from saccharomyces cerevisiae simultaneously influences cyclization, rearrangement, and deprotonation reactions. Chembiochem 6(7):1177-81
Mullner H, et al.  (2004) Targeting of proteins involved in sterol biosynthesis to lipid particles of the yeast Saccharomyces cerevisiae. Biochim Biophys Acta 1663(1-2):9-13
Athenstaedt K, et al.  (1999) Identification and characterization of major lipid particle proteins of the yeast Saccharomyces cerevisiae. J Bacteriol 181(20):6441-8
Corey EJ, et al.  (1994) Molecular cloning, characterization, and overexpression of ERG7, the Saccharomyces cerevisiae gene encoding lanosterol synthase. Proc Natl Acad Sci U S A 91(6):2211-5
Shi Z, et al.  (1994) Isolation and characterization of the gene encoding 2,3-oxidosqualene-lanosterol cyclase from Saccharomyces cerevisiae. Proc Natl Acad Sci U S A 91(15):7370-4